8ynm

Electron Microscopy
3.49Å resolution

Structure of the Caspase-8/cFLIP death effector domain assembly

Released:

Function and Biology Details

Reaction catalysed:
Strict requirement for Asp at position P1 and has a preferred cleavage sequence of (Leu/Asp/Val)-Glu-Thr-Asp-|-(Gly/Ser/Ala)
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero undecamer (preferred)
PDBe Complex ID:
PDB-CPX-518598 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
CASP8 and FADD-like apoptosis regulator subunit p43 Chains: F, G, H, I, J, K, N, O
Molecule details ›
Chains: F, G, H, I, J, K, N, O
Length: 181 amino acids
Theoretical weight: 20.88 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O15519 (Residues: 1-181; Coverage: 38%)
Gene names: CASH, CASP8AP1, CFLAR, CLARP, MRIT
Sequence domains: Death effector domain
Caspase-8 Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 479 amino acids
Theoretical weight: 55.19 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q14790 (Residues: 1-479; Coverage: 100%)
Gene names: CASP8, MCH5
Sequence domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 3.49Å
Relevant EMDB volumes: EMD-39427
Expression system: Escherichia coli